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Published December 1, 1972 | public
Journal Article Open

Partial Characterization of a Tetrodotoxin-Binding Component from Nerve Membrane


Tetrodotoxin from Japanese puffer fish has been labeled with tritium and purified from the crude mixture obtained. The interaction between the purified [3H]tetrodotoxin and membrane suspensions from the olfactory nerve of long-nosed garfish has been investigated by equilibrium dialysis. Tetrodotoxin binds to membrane suspensions with a dissociation constant KD = 8.3 nM. The nerve preparation binds 42 pmol of [3H]tetrodotoxin/g of wet tissue at saturating toxin concentrations. With various hydrolytic enzymes, the binding component is shown to be a protein embedded in a phospholipid environment. The binding is inhibited below pH 4.0 and is not stable towards heat. Tetrodotoxin binding is not inhibited by the local anesthetic, procaine.

Additional Information

Copyright © 1972 by the National Academy of Sciences Communicated by Daniel E. Koshland, Jr., September 29, 1972 We thank J. Racs and the turtles for putting up with the live garfish for so many months. Contribution no. 4533 from the Church Laboratory of Chemical Biology, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, Calif. 91109. M.A.R. is a recipient of National Institutes of Health Career Development Award.


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